1bx2

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(New page: 200px<br /> <applet load="1bx2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bx2, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1bx2.gif|left|200px]]<br /><applet load="1bx2" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1bx2" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1bx2, resolution 2.6&Aring;" />
caption="1bx2, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101,DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN'''<br />
'''CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101,DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN'''<br />
==Overview==
==Overview==
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Susceptibility to multiple sclerosis is associated with the human, histocompatibility leukocyte antigen (HLA)-DR2 (DRB1*1501) haplotype. The, structure of HLA-DR2 was determined with a bound peptide from human myelin, basic protein (MBP) that is immunodominant for human MBP-specific T cells., Residues of MBP peptide that are important for T cell receptor recognition, are prominent, solvent exposed residues in the crystal structure. A, distinguishing feature of the HLA-DR2 peptide binding site is a large, primarily hydrophobic P4 pocket that accommodates a phenylalanine of the, MBP peptide. The necessary space for this aromatic side chain is created, by an alanine at the polymorphic DRbeta 71 position. These features make, the P4 pocket of HLA-DR2 distinct from DR molecules associated with other, autoimmune diseases.
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Susceptibility to multiple sclerosis is associated with the human histocompatibility leukocyte antigen (HLA)-DR2 (DRB1*1501) haplotype. The structure of HLA-DR2 was determined with a bound peptide from human myelin basic protein (MBP) that is immunodominant for human MBP-specific T cells. Residues of MBP peptide that are important for T cell receptor recognition are prominent, solvent exposed residues in the crystal structure. A distinguishing feature of the HLA-DR2 peptide binding site is a large, primarily hydrophobic P4 pocket that accommodates a phenylalanine of the MBP peptide. The necessary space for this aromatic side chain is created by an alanine at the polymorphic DRbeta 71 position. These features make the P4 pocket of HLA-DR2 distinct from DR molecules associated with other autoimmune diseases.
==About this Structure==
==About this Structure==
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1BX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BX2 OCA].
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1BX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BX2 OCA].
==Reference==
==Reference==
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[[Category: Gauthier, L.]]
[[Category: Gauthier, L.]]
[[Category: Pyrdol, J.]]
[[Category: Pyrdol, J.]]
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[[Category: Smith, K.J.]]
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[[Category: Smith, K J.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: Wucherpfennig, K.]]
[[Category: Wucherpfennig, K.]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: myelin basic protein]]
[[Category: myelin basic protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:00 2008''

Revision as of 10:00, 21 February 2008


1bx2, resolution 2.6Å

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CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101,DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN

Overview

Susceptibility to multiple sclerosis is associated with the human histocompatibility leukocyte antigen (HLA)-DR2 (DRB1*1501) haplotype. The structure of HLA-DR2 was determined with a bound peptide from human myelin basic protein (MBP) that is immunodominant for human MBP-specific T cells. Residues of MBP peptide that are important for T cell receptor recognition are prominent, solvent exposed residues in the crystal structure. A distinguishing feature of the HLA-DR2 peptide binding site is a large, primarily hydrophobic P4 pocket that accommodates a phenylalanine of the MBP peptide. The necessary space for this aromatic side chain is created by an alanine at the polymorphic DRbeta 71 position. These features make the P4 pocket of HLA-DR2 distinct from DR molecules associated with other autoimmune diseases.

About this Structure

1BX2 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein., Smith KJ, Pyrdol J, Gauthier L, Wiley DC, Wucherpfennig KW, J Exp Med. 1998 Oct 19;188(8):1511-20. PMID:9782128

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